ID   SYP_CHLTR               Reviewed;         581 AA.
AC   P36431; O84398;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   25-MAY-2022, entry version 132.
DE   RecName: Full=Proline--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_01569};
DE            EC=6.1.1.15 {ECO:0000255|HAMAP-Rule:MF_01569};
DE   AltName: Full=Prolyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_01569};
DE            Short=ProRS {ECO:0000255|HAMAP-Rule:MF_01569};
GN   Name=proS {ECO:0000255|HAMAP-Rule:MF_01569}; OrderedLocusNames=CT_393;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=E/UW-5/Cx;
RX   PubMed=8045424; DOI=10.1016/0378-1119(94)90322-0;
RA   Schmiel D.H., Wyrick P.B.;
RT   "Another putative heat-shock gene and aminoacyl-tRNA synthetase gene are
RT   located upstream from the grpE-like and dnaK-like genes in Chlamydia
RT   trachomatis.";
RL   Gene 145:57-63(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
CC   -!- FUNCTION: Catalyzes the attachment of proline to tRNA(Pro) in a two-
CC       step reaction: proline is first activated by ATP to form Pro-AMP and
CC       then transferred to the acceptor end of tRNA(Pro). As ProRS can
CC       inadvertently accommodate and process non-cognate amino acids such as
CC       alanine and cysteine, to avoid such errors it has two additional
CC       distinct editing activities against alanine. One activity is designated
CC       as 'pretransfer' editing and involves the tRNA(Pro)-independent
CC       hydrolysis of activated Ala-AMP. The other activity is designated
CC       'posttransfer' editing and involves deacylation of mischarged Ala-
CC       tRNA(Pro). The misacylated Cys-tRNA(Pro) is not edited by ProRS.
CC       {ECO:0000255|HAMAP-Rule:MF_01569}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-proline + tRNA(Pro) = AMP + diphosphate + L-prolyl-
CC         tRNA(Pro); Xref=Rhea:RHEA:14305, Rhea:RHEA-COMP:9700, Rhea:RHEA-
CC         COMP:9702, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:60039,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78532, ChEBI:CHEBI:456215;
CC         EC=6.1.1.15; Evidence={ECO:0000255|HAMAP-Rule:MF_01569};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01569}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01569}.
CC   -!- DOMAIN: Consists of three domains: the N-terminal catalytic domain, the
CC       editing domain and the C-terminal anticodon-binding domain.
CC       {ECO:0000255|HAMAP-Rule:MF_01569}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       ProS type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_01569}.
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DR   EMBL; L25105; AAA23161.1; -; Genomic_DNA.
DR   EMBL; AE001273; AAC67990.1; -; Genomic_DNA.
DR   PIR; G71520; G71520.
DR   RefSeq; NP_219903.1; NC_000117.1.
DR   RefSeq; WP_010725180.1; NC_000117.1.
DR   AlphaFoldDB; P36431; -.
DR   SMR; P36431; -.
DR   STRING; 813.O172_02140; -.
DR   EnsemblBacteria; AAC67990; AAC67990; CT_393.
DR   GeneID; 884722; -.
DR   KEGG; ctr:CT_393; -.
DR   PATRIC; fig|272561.5.peg.423; -.
DR   HOGENOM; CLU_016739_0_0_0; -.
DR   InParanoid; P36431; -.
DR   OMA; NCDYAAN; -.
DR   Proteomes; UP000000431; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004827; F:proline-tRNA ligase activity; IBA:GO_Central.
DR   GO; GO:0006433; P:prolyl-tRNA aminoacylation; IBA:GO_Central.
DR   CDD; cd00861; ProRS_anticodon_short; 1.
DR   CDD; cd00779; ProRS_core_prok; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   Gene3D; 3.40.50.800; -; 1.
DR   Gene3D; 3.90.960.10; -; 1.
DR   HAMAP; MF_01569; Pro_tRNA_synth_type1; 1.
DR   InterPro; IPR002314; aa-tRNA-synt_IIb.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR004154; Anticodon-bd.
DR   InterPro; IPR036621; Anticodon-bd_dom_sf.
DR   InterPro; IPR002316; Pro-tRNA-ligase_IIa.
DR   InterPro; IPR004500; Pro-tRNA-synth_IIa_bac-type.
DR   InterPro; IPR023717; Pro-tRNA-Synthase_IIa_type1.
DR   InterPro; IPR044140; ProRS_anticodon_short.
DR   InterPro; IPR033730; ProRS_core_prok.
DR   InterPro; IPR036754; YbaK/aa-tRNA-synt-asso_dom_sf.
DR   InterPro; IPR007214; YbaK/aa-tRNA-synth-assoc-dom.
DR   Pfam; PF03129; HGTP_anticodon; 1.
DR   Pfam; PF00587; tRNA-synt_2b; 1.
DR   Pfam; PF04073; tRNA_edit; 1.
DR   PRINTS; PR01046; TRNASYNTHPRO.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   SUPFAM; SSF55826; SSF55826; 1.
DR   TIGRFAMs; TIGR00409; proS_fam_II; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..581
FT                   /note="Proline--tRNA ligase"
FT                   /id="PRO_0000139327"
FT   VARIANT         3
FT                   /note="M -> T (in strain: E/UW-5/Cx)"
FT   VARIANT         14
FT                   /note="A -> V (in strain: E/UW-5/Cx)"
FT   VARIANT         104
FT                   /note="K -> E (in strain: E/UW-5/Cx)"
FT   VARIANT         263
FT                   /note="I -> V (in strain: E/UW-5/Cx)"
FT   VARIANT         286
FT                   /note="C -> R (in strain: E/UW-5/Cx)"
FT   VARIANT         354
FT                   /note="P -> L (in strain: E/UW-5/Cx)"
SQ   SEQUENCE   581 AA;  65653 MW;  08815CF98623F259 CRC64;
     MRMSLLFYRT SKNANKEASV LSYELLQKAG YLFKTSKGIY SYTPLFQRVI LKMTEIIREE
     LNAIGGQEVC LPLLQPAELW EKTGRWKAFL SEKLLYVLKD RENKAMCLAP THEEVVSEFV
     AQWLTGREQL PIHLYQIGTK FRDEIRPRFG LMRAKEFLME DSYTFSDSPE QMEEQYAKLR
     LAYQRIFDRL NLKYVIVAAD GGKIGKGKSE EFHVLCSLGE DTICVSGSYG ANVEAAQAIP
     PSYVYDSNLL PVEEVATPNI RTIEDLEVFF NTPKHKILKT LVVKTCQKDS EKFFAICIRG
     DRQINLTKVA SFLQVDDCEL ASEEEILKHL HVEKGFIGPL YCPIPCYADE TTRPMTNFIC
     ANNQKDVHCK HVNWGRDIPL PAFGDFLLAE AGDLCPQNGG APYEIFQGVE VAHIFNLGTR
     YTESFSVGFQ DKNGDKQLCW MGTYGIGVGR TLAACIEQLA DNKGLVWPLA VAPFSITILY
     NGGDTEGEAT ALQLYQSLNT EGFEPLLDDR NERLGFKLKD SDLLGIPYKL IIGKSFQSTG
     LLEIESRSGE KCNVSPENLL DWCSKNLPCH TRKIPPLREQ N